Proteins of human urine. III. Identification and two-dimensional electrophoretic map positions of some major urinary proteins.
We mapped the proteins of human urine by high-resolution two-dimensional electrophoresis, utilizing the ISO-DALT system. Wide-range pH gradients and narrow-range acid gradients were both used in the first-dimension separations. The patterns revealed proteins ranging in relative molecular mass from 10 000 to 90 000. Proteins identified in the map included transferrin, albumin, hemopexin, alpha 2-HS glycoprotein, alpha 1-antitrypsin. Gc globulin, alpha 1-acid glycoprotein, Zn alpha 2-glycoprotein, retinol binding protein, beta 2-microglobulin, the immunoglobulin light chains, and MAUP (most acid urinary protein). The use and utility of internal-charge and molecular-mass standards are described. We used electrophoretic transfer of proteins to nitrocellulose sheets and subsequent detection by immunological methods to identify some proteins.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006736:Horses; D006801:Humans; D007145:Immunoglobulin kappa-Chains / Q000032:analysis; D007146:Immunoglobulin lambda-Chains / Q000032:analysis; D007525:Isoelectric Focusing; D008297:Male; D008970:Molecular Weight; D009101:Multiple Myeloma / Q000652:urine; D011506:Proteins / Q000032:analysis*; D011507:Proteinuria / Q000652:urine*; D011817:Rabbits
D007145:Immunoglobulin kappa-Chains; D007146:Immunoglobulin lambda-Chains; D011506:Proteins